Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

Gene

ALG6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man9GlcNAc(2)-PP-Dol.

Catalytic activityi

Dolichyl beta-D-glucosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.267. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_267765. Defective ALG6 causes ALG6-CDG (CDG-1c).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC:2.4.1.267)
Alternative name(s):
Asparagine-linked glycosylation protein 6 homolog
Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene namesi
Name:ALG6
ORF Names:My046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:23157. ALG6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4 – 2421HelicalSequence AnalysisAdd
BLAST
Transmembranei115 – 13521HelicalSequence AnalysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence AnalysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Transmembranei298 – 31821HelicalSequence AnalysisAdd
BLAST
Transmembranei324 – 34421HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Transmembranei438 – 45821HelicalSequence AnalysisAdd
BLAST
Transmembranei473 – 49321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: GO_Central
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1C (CDG1C)7 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

See also OMIM:603147
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311Y → H in CDG1C. 2 Publications
Corresponds to variant rs35383149 [ dbSNP | Ensembl ].
VAR_022511
Natural varianti170 – 1701S → I in CDG1C. 1 Publication
VAR_022512
Natural varianti227 – 2271G → E in CDG1C. 1 Publication
VAR_022513
Natural varianti299 – 2991Missing in CDG1C. 1 Publication
VAR_013441
Natural varianti308 – 3081S → R in CDG1C. 1 Publication
VAR_022514
Natural varianti333 – 3331A → V in CDG1C. 3 Publications
VAR_013443
Natural varianti444 – 4441Missing in CDG1C. 1 Publication
VAR_022515
Natural varianti478 – 4781S → P in CDG1C. 1 Publication
VAR_013444

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi603147. phenotype.
Orphaneti79320. ALG6-CDG.
PharmGKBiPA134925619.

Polymorphism and mutation databases

BioMutaiALG6.
DMDMi21263380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferasePRO_0000174156Add
BLAST

Proteomic databases

MaxQBiQ9Y672.
PaxDbiQ9Y672.
PRIDEiQ9Y672.

PTM databases

PhosphoSiteiQ9Y672.

Expressioni

Gene expression databases

BgeeiQ9Y672.
CleanExiHS_ALG6.
ExpressionAtlasiQ9Y672. baseline and differential.
GenevestigatoriQ9Y672.

Interactioni

Protein-protein interaction databases

BioGridi118970. 3 interactions.
STRINGi9606.ENSP00000360149.

Structurei

3D structure databases

ProteinModelPortaliQ9Y672.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287760.
HOGENOMiHOG000195048.
HOVERGENiHBG024331.
InParanoidiQ9Y672.
KOiK03848.
OrthoDBiEOG70088D.
PhylomeDBiQ9Y672.
TreeFamiTF314522.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 1 hit.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKWYLMTVV VLIGLTVRWT VSLNSYSGAG KPPMFGDYEA QRHWQEITFN
60 70 80 90 100
LPVKQWYFNS SDNNLQYWGL DYPPLTAYHS LLCAYVAKFI NPDWIALHTS
110 120 130 140 150
RGYESQAHKL FMRTTVLIAD LLIYIPAVVL YCCCLKEIST KKKIANALCI
160 170 180 190 200
LLYPGLILID YGHFQYNSVS LGFALWGVLG ISCDCDLLGS LAFCLAINYK
210 220 230 240 250
QMELYHALPF FCFLLGKCFK KGLKGKGFVL LVKLACIVVA SFVLCWLPFF
260 270 280 290 300
TEREQTLQVL RRLFPVDRGL FEDKVANIWC SFNVFLKIKD ILPRHIQLIM
310 320 330 340 350
SFCFTFLSLL PACIKLILQP SSKGFKFTLV SCALSFFLFS FQVHEKSILL
360 370 380 390 400
VSLPVCLVLS EIPFMSTWFL LVSTFSMLPL LLKDELLMPS VVTTMAFFIA
410 420 430 440 450
CVTSFSIFEK TSEEELQLKS FSISVRKYLP CFTFLSRIIQ YLFLISVITM
460 470 480 490 500
VLLTLMTVTL DPPQKLPDLF SVLVCFVSCL NFLFFLVYFN IIIMWDSKSG

RNQKKIS
Length:507
Mass (Da):58,181
Last modified:November 1, 1999 - v1
Checksum:i6558E0A318597D03
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111F → L in AAG43163 (Ref. 2) Curated
Sequence conflicti374 – 3741T → P in AAG43163 (Ref. 2) Curated
Sequence conflicti394 – 3941T → P in AAG43163 (Ref. 2) Curated
Sequence conflicti457 – 4571T → A in AAG43163 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311Y → H in CDG1C. 2 Publications
Corresponds to variant rs35383149 [ dbSNP | Ensembl ].
VAR_022511
Natural varianti170 – 1701S → I in CDG1C. 1 Publication
VAR_022512
Natural varianti226 – 2261K → N.
Corresponds to variant rs35604168 [ dbSNP | Ensembl ].
VAR_055493
Natural varianti227 – 2271G → E in CDG1C. 1 Publication
VAR_022513
Natural varianti299 – 2991Missing in CDG1C. 1 Publication
VAR_013441
Natural varianti304 – 3041F → S Common polymorphism; may exacerbate the clinical severity of patients with CDG1A; reduces the ability to rescue defective glycosylation of an alg6-deficient strain of S. cerevisiae during rapid growth. 5 Publications
Corresponds to variant rs4630153 [ dbSNP | Ensembl ].
VAR_013442
Natural varianti308 – 3081S → R in CDG1C. 1 Publication
VAR_022514
Natural varianti333 – 3331A → V in CDG1C. 3 Publications
VAR_013443
Natural varianti444 – 4441Missing in CDG1C. 1 Publication
VAR_022515
Natural varianti478 – 4781S → P in CDG1C. 1 Publication
VAR_013444

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102851 mRNA. Translation: AAD41466.1.
AF063604 mRNA. Translation: AAG43163.1.
AK022700 mRNA. Translation: BAG51104.1.
AL592218, AL049636 Genomic DNA. Translation: CAI18961.1.
AL049636, AL592218 Genomic DNA. Translation: CAI22829.1.
CH471059 Genomic DNA. Translation: EAX06571.1.
BC001253 mRNA. Translation: AAH01253.1.
CCDSiCCDS30735.1.
RefSeqiNP_037471.2. NM_013339.3.
UniGeneiHs.258501.

Genome annotation databases

EnsembliENST00000371108; ENSP00000360149; ENSG00000088035.
GeneIDi29929.
KEGGihsa:29929.
UCSCiuc021oof.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102851 mRNA. Translation: AAD41466.1.
AF063604 mRNA. Translation: AAG43163.1.
AK022700 mRNA. Translation: BAG51104.1.
AL592218, AL049636 Genomic DNA. Translation: CAI18961.1.
AL049636, AL592218 Genomic DNA. Translation: CAI22829.1.
CH471059 Genomic DNA. Translation: EAX06571.1.
BC001253 mRNA. Translation: AAH01253.1.
CCDSiCCDS30735.1.
RefSeqiNP_037471.2. NM_013339.3.
UniGeneiHs.258501.

3D structure databases

ProteinModelPortaliQ9Y672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118970. 3 interactions.
STRINGi9606.ENSP00000360149.

Protein family/group databases

CAZyiGT57. Glycosyltransferase Family 57.

PTM databases

PhosphoSiteiQ9Y672.

Polymorphism and mutation databases

BioMutaiALG6.
DMDMi21263380.

Proteomic databases

MaxQBiQ9Y672.
PaxDbiQ9Y672.
PRIDEiQ9Y672.

Protocols and materials databases

DNASUi29929.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371108; ENSP00000360149; ENSG00000088035.
GeneIDi29929.
KEGGihsa:29929.
UCSCiuc021oof.1. human.

Organism-specific databases

CTDi29929.
GeneCardsiGC01P063834.
H-InvDBHIX0000661.
HGNCiHGNC:23157. ALG6.
MIMi603147. phenotype.
604566. gene.
neXtProtiNX_Q9Y672.
Orphaneti79320. ALG6-CDG.
PharmGKBiPA134925619.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG287760.
HOGENOMiHOG000195048.
HOVERGENiHBG024331.
InParanoidiQ9Y672.
KOiK03848.
OrthoDBiEOG70088D.
PhylomeDBiQ9Y672.
TreeFamiTF314522.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.267. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_267765. Defective ALG6 causes ALG6-CDG (CDG-1c).

Miscellaneous databases

ChiTaRSiALG6. human.
GeneWikiiALG6.
GenomeRNAii29929.
NextBioi52559.
PROiQ9Y672.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y672.
CleanExiHS_ALG6.
ExpressionAtlasiQ9Y672. baseline and differential.
GenevestigatoriQ9Y672.

Family and domain databases

InterProiIPR004856. Glyco_trans_ALG6/ALG8.
[Graphical view]
PANTHERiPTHR12413. PTHR12413. 1 hit.
PfamiPF03155. Alg6_Alg8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic."
    Imbach T., Burda P., Kuhnert P., Wevers R.A., Aebi M., Berger E.G., Hennet T.
    Proc. Natl. Acad. Sci. U.S.A. 96:6982-6987(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CDG1C VAL-333.
  2. Mao Y.M., Xie Y., Zheng Z.H.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-304.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. "Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation."
    Westphal V., Murch S., Kim S., Srikrishna G., Winchester B., Day R., Freeze H.H.
    Am. J. Pathol. 157:1917-1925(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1C HIS-131; ARG-308 AND VAL-333.
  8. Cited for: VARIANTS CDG1C VAL-333 AND PRO-478, VARIANT SER-304.
  9. "Analysis of multiple mutations in the hALG6 gene in a patient with congenital disorder of glycosylation Ic."
    Westphal V., Schottstaedt C., Marquardt T., Freeze H.H.
    Mol. Genet. Metab. 70:219-223(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C ILE-299 DEL, VARIANT SER-304.
  10. "The T911C (F304S) substitution in the human ALG6 gene is a common polymorphism and not a causal mutation of CDG-Ic."
    Vuillaumier-Barrot S., Le Bizec C., Durand G., Seta N.
    J. Hum. Genet. 46:547-548(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-304.
  11. Cited for: VARIANTS CDG1C ILE-170 AND LEU-444 DEL.
  12. "DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG)."
    Schollen E., Martens K., Geuzens E., Matthijs G.
    Eur. J. Hum. Genet. 10:643-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C GLU-227.
  13. "A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency."
    Westphal V., Kjaergaard S., Schollen E., Martens K., Gruenewald S., Schwartz M., Matthijs G., Freeze H.H.
    Hum. Mol. Genet. 11:599-604(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT SER-304.
  14. "Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic."
    Westphal V., Xiao M., Kwok P.-Y., Freeze H.H.
    Hum. Mutat. 22:420-421(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1C HIS-131.

Entry informationi

Entry nameiALG6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y672
Secondary accession number(s): B3KMU2, Q5SXR9, Q9H3I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 1, 1999
Last modified: April 29, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.